2. Academic Validation
  3. Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240

Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240

  • Biomol NMR Assign. 2010 Apr;4(1):37-40. doi: 10.1007/s12104-009-9201-5.
Adam W Barb 1,  Ling Jiang,  Christian R H Raetz,  Pei Zhou
Affiliations

Affiliation

  • 1 Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
PMID: 19941092 DOI: 10.1007/s12104-009-9201-5
Abstract

The UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase LpxC catalyzes the committed reaction of lipid A biosynthesis, an essential pathway in Gram-negative bacteria. We report the backbone resonance assignments of the 34 kDa LpxC from Escherichia coli in complex with the Antibiotic L-161,240 using multidimensional, multinuclear NMR experiments. The (1)H chemical shifts of complexed L-161,240 are also determined.

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